Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6GYO

Structure of human HCN4 hyperpolarization-activated cyclic nucleotide-gated ion channel in complex with cAMP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005216	molecular_function	monoatomic ion channel activity
A	0005249	molecular_function	voltage-gated potassium channel activity
A	0006811	biological_process	monoatomic ion transport
A	0006813	biological_process	potassium ion transport
A	0016020	cellular_component	membrane
A	0055085	biological_process	transmembrane transport
B	0005216	molecular_function	monoatomic ion channel activity
B	0005249	molecular_function	voltage-gated potassium channel activity
B	0006811	biological_process	monoatomic ion transport
B	0006813	biological_process	potassium ion transport
B	0016020	cellular_component	membrane
B	0055085	biological_process	transmembrane transport
C	0005216	molecular_function	monoatomic ion channel activity
C	0005249	molecular_function	voltage-gated potassium channel activity
C	0006811	biological_process	monoatomic ion transport
C	0006813	biological_process	potassium ion transport
C	0016020	cellular_component	membrane
C	0055085	biological_process	transmembrane transport
D	0005216	molecular_function	monoatomic ion channel activity
D	0005249	molecular_function	voltage-gated potassium channel activity
D	0006811	biological_process	monoatomic ion transport
D	0006813	biological_process	potassium ion transport
D	0016020	cellular_component	membrane
D	0055085	biological_process	transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue CMP A 801

Chain	Residue
A	PHE658
A	ARG713
A	ILE714
A	GLY659
A	GLU660
A	ILE661
A	CYS662
A	ARG669
A	THR670
A	ALA671
A	ARG710

site_id	AC2
Number of Residues	6
Details	binding site for residue PC1 A 809

Chain	Residue
A	TRP341
A	LEU388
A	SER392
A	ILE395
A	TRP431
A	PC1805

site_id	AC3
Number of Residues	5
Details	binding site for residue PC1 A 803

Chain	Residue
A	SER460
A	TRP461
A	GLY462
A	TYR465
B	PC1808

site_id	AC4
Number of Residues	5
Details	binding site for residue PC1 A 804

Chain	Residue
A	THR504
A	MET508
D	MET476
D	LEU516
D	PC1804

site_id	AC5
Number of Residues	4
Details	binding site for residue PC1 A 805

Chain	Residue
A	HIS399
A	ASP432
A	3PE811
A	PC1809

site_id	AC6
Number of Residues	9
Details	binding site for residue PIE A 812

Chain	Residue
A	ASN227
A	PHE229
A	SER259
A	ASP260
A	PHE263
A	TYR264
A	ILE404
A	PHE405
A	MET407

site_id	AC7
Number of Residues	8
Details	binding site for residue 3PE A 810

Chain	Residue
A	LEU271
A	PHE287
A	GLU290
A	THR292
A	TRP295
A	PHE298
A	TYR465
A	3PE811

site_id	AC8
Number of Residues	7
Details	binding site for residue 3PE A 811

Chain	Residue
A	HIS399
A	ARG417
A	ASN420
A	MET424
A	MET508
A	PC1805
A	3PE810

site_id	AC9
Number of Residues	1
Details	binding site for residue PC1 A 806

Chain	Residue
B	PC1806

site_id	AD1
Number of Residues	4
Details	binding site for residue PC1 A 807

Chain	Residue
A	GLN443
A	SER490
A	PC1808
D	PC1806

site_id	AD2
Number of Residues	5
Details	binding site for residue PC1 A 808

Chain	Residue
A	ARG375
A	ARG378
A	ILE382
A	LEU442
A	PC1807

site_id	AD3
Number of Residues	4
Details	binding site for residue PC1 B 808

Chain	Residue
A	PC1803
B	GLN443
B	SER490
B	PC1809

site_id	AD4
Number of Residues	4
Details	binding site for residue PC1 B 809

Chain	Residue
B	ARG375
B	ARG378
B	LEU442
B	PC1808

site_id	AD5
Number of Residues	11
Details	binding site for residue CMP B 801

Chain	Residue
B	PHE658
B	GLY659
B	GLU660
B	ILE661
B	CYS662
B	ARG669
B	THR670
B	ALA671
B	ARG710
B	ARG713
B	ILE714

site_id	AD6
Number of Residues	6
Details	binding site for residue PC1 B 804

Chain	Residue
B	TRP341
B	LEU388
B	SER392
B	ILE395
B	TRP431
B	PC1807

site_id	AD7
Number of Residues	5
Details	binding site for residue PC1 B 805

Chain	Residue
B	SER460
B	TRP461
B	GLY462
B	TYR465
C	PC1808

site_id	AD8
Number of Residues	6
Details	binding site for residue PC1 B 806

Chain	Residue
B	THR504
B	MET508
A	LEU426
A	MET476
A	LEU516
A	PC1806

site_id	AD9
Number of Residues	4
Details	binding site for residue PC1 B 807

Chain	Residue
B	HIS399
B	ASP432
B	PC1804
B	3PE810

site_id	AE1
Number of Residues	9
Details	binding site for residue PIE B 812

Chain	Residue
B	ASN227
B	PHE229
B	SER259
B	ASP260
B	PHE263
B	TYR264
B	ILE404
B	PHE405
B	MET407

site_id	AE2
Number of Residues	8
Details	binding site for residue 3PE B 811

Chain	Residue
B	LEU271
B	PHE287
B	GLU290
B	THR292
B	TRP295
B	PHE298
B	TYR465
B	3PE810

site_id	AE3
Number of Residues	7
Details	binding site for residue 3PE B 810

Chain	Residue
B	HIS399
B	ARG417
B	ASN420
B	MET424
B	MET508
B	PC1807
B	3PE811

site_id	AE4
Number of Residues	1
Details	binding site for residue PC1 B 803

Chain	Residue
C	PC1806

site_id	AE5
Number of Residues	4
Details	binding site for residue PC1 C 808

Chain	Residue
B	PC1805
C	GLN443
C	SER490
C	PC1809

site_id	AE6
Number of Residues	4
Details	binding site for residue PC1 C 809

Chain	Residue
C	ARG375
C	ARG378
C	LEU442
C	PC1808

site_id	AE7
Number of Residues	11
Details	binding site for residue CMP C 801

Chain	Residue
C	PHE658
C	GLY659
C	GLU660
C	ILE661
C	CYS662
C	ARG669
C	THR670
C	ALA671
C	ARG710
C	ARG713
C	ILE714

site_id	AE8
Number of Residues	6
Details	binding site for residue PC1 C 804

Chain	Residue
C	TRP341
C	LEU388
C	SER392
C	ILE395
C	TRP431
C	PC1807

site_id	AE9
Number of Residues	5
Details	binding site for residue PC1 C 805

Chain	Residue
C	SER460
C	TRP461
C	GLY462
C	TYR465
D	PC1809

site_id	AF1
Number of Residues	5
Details	binding site for residue PC1 C 806

Chain	Residue
B	LEU426
B	LEU516
B	PC1803
C	THR504
C	MET508

site_id	AF2
Number of Residues	4
Details	binding site for residue PC1 C 807

Chain	Residue
C	HIS399
C	ASP432
C	PC1804
C	3PE810

site_id	AF3
Number of Residues	9
Details	binding site for residue PIE C 812

Chain	Residue
C	ASN227
C	PHE229
C	SER259
C	ASP260
C	PHE263
C	TYR264
C	ILE404
C	PHE405
C	MET407

site_id	AF4
Number of Residues	8
Details	binding site for residue 3PE C 811

Chain	Residue
C	LEU271
C	PHE287
C	GLU290
C	THR292
C	TRP295
C	PHE298
C	TYR465
C	3PE810

site_id	AF5
Number of Residues	7
Details	binding site for residue 3PE C 810

Chain	Residue
C	HIS399
C	ARG417
C	ASN420
C	MET424
C	MET508
C	PC1807
C	3PE811

site_id	AF6
Number of Residues	1
Details	binding site for residue PC1 C 803

Chain	Residue
D	PC1807

site_id	AF7
Number of Residues	1
Details	binding site for residue PC1 D 804

Chain	Residue
A	PC1804

site_id	AF8
Number of Residues	4
Details	binding site for residue PC1 D 809

Chain	Residue
C	PC1805
D	GLN443
D	SER490
D	PC1803

site_id	AF9
Number of Residues	4
Details	binding site for residue PC1 D 803

Chain	Residue
D	ARG375
D	ARG378
D	LEU442
D	PC1809

site_id	AG1
Number of Residues	11
Details	binding site for residue CMP D 801

Chain	Residue
D	PHE658
D	GLY659
D	GLU660
D	ILE661
D	CYS662
D	ARG669
D	THR670
D	ALA671
D	ARG710
D	ARG713
D	ILE714

site_id	AG2
Number of Residues	6
Details	binding site for residue PC1 D 805

Chain	Residue
D	TRP341
D	LEU388
D	SER392
D	ILE395
D	TRP431
D	PC1808

site_id	AG3
Number of Residues	5
Details	binding site for residue PC1 D 806

Chain	Residue
A	PC1807
D	SER460
D	TRP461
D	GLY462
D	TYR465

site_id	AG4
Number of Residues	5
Details	binding site for residue PC1 D 807

Chain	Residue
C	LEU426
C	LEU516
C	PC1803
D	THR504
D	MET508

site_id	AG5
Number of Residues	4
Details	binding site for residue PC1 D 808

Chain	Residue
D	HIS399
D	ASP432
D	PC1805
D	3PE811

site_id	AG6
Number of Residues	9
Details	binding site for residue PIE D 812

Chain	Residue
D	ASN227
D	PHE229
D	SER259
D	ASP260
D	PHE263
D	TYR264
D	ILE404
D	PHE405
D	MET407

site_id	AG7
Number of Residues	8
Details	binding site for residue 3PE D 810

Chain	Residue
D	LEU271
D	PHE287
D	GLU290
D	THR292
D	TRP295
D	PHE298
D	TYR465
D	3PE811

site_id	AG8
Number of Residues	7
Details	binding site for residue 3PE D 811

Chain	Residue
D	HIS399
D	ARG417
D	ASN420
D	MET424
D	MET508
D	PC1808
D	3PE810

Functional Information from PROSITE/UniProt

site_id	PS00888
Number of Residues	17
Details	CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. IIrEGTiGKkMYFIqhG

Chain	Residue	Details
A	ILE622-GLY638

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	88
Details	Transmembrane: {"description":"Helical; Name=Segment S1","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2018","submissionDatabase":"PDB data bank","title":"Structure of human HCN4 hyperpolarization-activated cyclic nucleotide-gated ion channel.","authors":["Shintre C.A.","Pike A.C.W.","Tessitore A.","Young M.","Bushell S.R.","Strain-Damerell C.","Mukhopadhyay S.","Burgess-Brown N.A.","Huiskonen J.T.","Arrowsmith C.H.","Edwards A.M.","Bountra C.","Carpenter E.P."]}},{"source":"PDB","id":"6GYN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	220
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	80
Details	Transmembrane: {"description":"Helical; Name=Segment S2","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2018","submissionDatabase":"PDB data bank","title":"Structure of human HCN4 hyperpolarization-activated cyclic nucleotide-gated ion channel.","authors":["Shintre C.A.","Pike A.C.W.","Tessitore A.","Young M.","Bushell S.R.","Strain-Damerell C.","Mukhopadhyay S.","Burgess-Brown N.A.","Huiskonen J.T.","Arrowsmith C.H.","Edwards A.M.","Bountra C.","Carpenter E.P."]}},{"source":"PDB","id":"6GYN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	136
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	88
Details	Transmembrane: {"description":"Helical; Name=Segment S3","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2018","submissionDatabase":"PDB data bank","title":"Structure of human HCN4 hyperpolarization-activated cyclic nucleotide-gated ion channel.","authors":["Shintre C.A.","Pike A.C.W.","Tessitore A.","Young M.","Bushell S.R.","Strain-Damerell C.","Mukhopadhyay S.","Burgess-Brown N.A.","Huiskonen J.T.","Arrowsmith C.H.","Edwards A.M.","Bountra C.","Carpenter E.P."]}},{"source":"PDB","id":"6GYN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	80
Details	Transmembrane: {"description":"Helical; Voltage-sensor; Name=Segment S4","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2018","submissionDatabase":"PDB data bank","title":"Structure of human HCN4 hyperpolarization-activated cyclic nucleotide-gated ion channel.","authors":["Shintre C.A.","Pike A.C.W.","Tessitore A.","Young M.","Bushell S.R.","Strain-Damerell C.","Mukhopadhyay S.","Burgess-Brown N.A.","Huiskonen J.T.","Arrowsmith C.H.","Edwards A.M.","Bountra C.","Carpenter E.P."]}},{"source":"PDB","id":"6GYN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	88
Details	Transmembrane: {"description":"Helical; Name=Segment S5","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2018","submissionDatabase":"PDB data bank","title":"Structure of human HCN4 hyperpolarization-activated cyclic nucleotide-gated ion channel.","authors":["Shintre C.A.","Pike A.C.W.","Tessitore A.","Young M.","Bushell S.R.","Strain-Damerell C.","Mukhopadhyay S.","Burgess-Brown N.A.","Huiskonen J.T.","Arrowsmith C.H.","Edwards A.M.","Bountra C.","Carpenter E.P."]}},{"source":"PDB","id":"6GYN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	84
Details	Intramembrane: {"description":"Pore-forming; Name=Segment H5","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	100
Details	Transmembrane: {"description":"Helical; Name=Segment S6","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2018","submissionDatabase":"PDB data bank","title":"Structure of human HCN4 hyperpolarization-activated cyclic nucleotide-gated ion channel.","authors":["Shintre C.A.","Pike A.C.W.","Tessitore A.","Young M.","Bushell S.R.","Strain-Damerell C.","Mukhopadhyay S.","Burgess-Brown N.A.","Huiskonen J.T.","Arrowsmith C.H.","Edwards A.M.","Bountra C.","Carpenter E.P."]}},{"source":"PDB","id":"6GYN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24776929","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4KL1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22006928","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23103389","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3U11","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HBN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9TV66","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22006928","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3U11","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23103389","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4HBN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)